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2j9t

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[[Category: type 3 secretion system]]
[[Category: type 3 secretion system]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:00:48 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 18:28:56 2007''

Revision as of 16:23, 5 November 2007

Image:2j9t.gif

2j9t, resolution 2.7Å

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BIPD OF BURKHOLDERIA PSEUDOMALLEI

Overview

Bacteria expressing type III secretion systems (T3SS) have been, responsible for the deaths of millions worldwide, acting as key virulence, elements in diseases ranging from plague to typhoid fever. The T3SS is, composed of a basal body, which traverses both bacterial membranes, and an, external needle through which effector proteins are secreted. We report, multiple crystal structures of two proteins that sit at the tip of the, needle and are essential for virulence: IpaD from Shigella flexneri and, BipD from Burkholderia pseudomallei. The structures reveal that the, N-terminal domains of the molecules are intramolecular chaperones that, prevent premature oligomerization, as well as sharing structural homology, with proteins involved in eukaryotic actin rearrangement. Crystal packing, has allowed us to construct a model for the tip complex that is supported, by mutations designed using the structure.

About this Structure

2J9T is a Single protein structure of sequence from Burkholderia pseudomallei with FLC and BO3 as ligands. This structure superseeds the now removed PDB entry 2CMQ. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD., Johnson S, Roversi P, Espina M, Olive A, Deane JE, Birket S, Field T, Picking WD, Blocker AJ, Galyov EE, Picking WL, Lea SM, J Biol Chem. 2007 Feb 9;282(6):4035-44. Epub 2006 Oct 31. PMID:17077085

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